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Database: UniProt
Entry: A0A011MD52_9PROT
LinkDB: A0A011MD52_9PROT
Original site: A0A011MD52_9PROT 
ID   A0A011MD52_9PROT        Unreviewed;       363 AA.
AC   A0A011MD52;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=rpfC {ECO:0000313|EMBL:EXI67693.1};
GN   ORFNames=AW07_04494 {ECO:0000313|EMBL:EXI67693.1};
OS   Candidatus Accumulibacter sp. SK-11.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1454000 {ECO:0000313|EMBL:EXI67693.1, ECO:0000313|Proteomes:UP000020226};
RN   [1] {ECO:0000313|EMBL:EXI67693.1, ECO:0000313|Proteomes:UP000020226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-11 {ECO:0000313|Proteomes:UP000020226};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXI67693.1}.
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DR   EMBL; JFAW01000054; EXI67693.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A011MD52; -.
DR   STRING; 1454000.AW07_04494; -.
DR   PATRIC; fig|1454000.3.peg.3641; -.
DR   Proteomes; UP000020226; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000020226};
KW   Transferase {ECO:0000313|EMBL:EXI67693.1}.
FT   DOMAIN          1..217
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          241..363
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         290
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   363 AA;  39002 MW;  92FE9732E66BF947 CRC64;
     MSHEIRTPMN GVLGMAELLL ATPLSVEQRS RLDTLHRSAR NLLDVINDVL DFSKIEAGKL
     DLRPGDFDLL QTVDEICGSL ATAAGSKGLL LSTAVEPDVP RFVNGDGARL RQVLINLVGN
     AIKFTDSGNI VVSLARSDER RLRFAVQDTG IGLTPAECEQ IFAAFAQADA SNTRRHGGTG
     LGLAISKRLV TLMGGIIGVD SLPGRGSTFW FEIPLLAVQP PSTDAPGSAA ASAAVRQLHA
     HVLLVEDNPV NQLVAQAFLE VLGLQVTLAE NGRQAVERWR AQRFDLILMD CQMPELDGFD
     ATRQIRAGEQ AAAAAGKAGI PIIALTANAF EADRERCLAS GMNDFIAKPF TQGELYRTLS
     RWI
//
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